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Application note: Characterizing protein oligomerization with automated mass photometry
Learn about the advantages of automated mass photometry for oligomerization studies. Read the application note and discover how the quick and repeatable measurements provided by the TwoMP Auto help characterize the factors that define oligomerization behavior. Look at the data from two case studies in which protein concentration or the presence of an effector is varied, and the treated samples are systematically characterized with automated mass photometry. Here, you will see how the single-molecule mass distributions provided by mass photometry can be used to identify the different oligomeric species in a sample.
Additional resources
BLOG: Blog: Studying protein oligomerization with mass photometry – insights from a future PI
In this blog post, we talk to Dr. Kathryn Gunn about her research into the oligomeric states of lipoprotein lipase and how its structure relates to its activity. Her team used mass photometry to analyze the LPL oligomeric states and structural changes in solution, while cryoEM was used to visualize LPL structures in thin ice layers. Cross-linking, mass spectrometry, and western blotting were also employed to further characterize LPL oligomers and protein interactions.
WEBINAR: Automated mass photometry: Easing the path to biomolecular characterization
In this webinar, we discuss in detail the automated mass photometry and show data on some of its most attractive applications—such as screening and titration assays. We illustrate how automation and the associated improvement in reproducibility can make biomolecular characterization – including protein oligomerization – with mass photometry even easier.
